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Literature summary extracted from

  • Preabrazhenskaya, Y.V.; Kim, I.Y.; Stadtman, T.C.
    Binding of ATP and its derivatives to selenophosphate synthetase from Escherichia coli (2009), Biochemistry (Moscow), 74, 910-916.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.9.3 into the vector pCR2.1 and subsequently into pKK233.2 for expression in Escherichia coli MB08 cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.9.3 C17S catalytically inactive mutant Escherichia coli
2.7.9.3 SPS238 C-terminally truncated mutant containing the N-terminal 238 amino acids of the 348-amino-acid protein Escherichia coli
2.7.9.3 SPS262 C-terminally truncated mutant containing the N-terminal 262 amino acids of the 348-amino-acid protein Escherichia coli
2.7.9.3 SPS332 C-terminally truncated mutant containing the N-terminal 332 amino acids of the 348-amino-acid protein Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.9.3 1.6
-
 ATP Mn-ATP, wild-type enzyme Escherichia coli
2.7.9.3 5.2
-
 ATP Mn-ATP, mutant SPS332 Escherichia coli
2.7.9.3 7.7
-
 ATP Mn-ATP, mutant SPS262 Escherichia coli
2.7.9.3 10.3
-
 ATP Mn-ATP, mutant SPS238 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.9.3 Mg2+
-
 Escherichia coli
2.7.9.3 Mn2+
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.9.3 25000
-
 mutant SPS238 Escherichia coli
2.7.9.3 29000
-
 mutant SPS262 Escherichia coli
2.7.9.3 34000
-
 mutant SPS332 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.9.3 ATP + selenide + H2O Escherichia coli
-
 AMP + selenophosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.9.3 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.9.3 DEAE-Sepharose chromatography is used after an ammonium sulfate fractionation step followed by phenyl-Sepharose and butyl-Sepharose chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.9.3 ATP + selenide + H2O
-
 Escherichia coli AMP + selenophosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.9.3 selenophosphate synthetase
-
 Escherichia coli
2.7.9.3 SPS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.9.3 37
-
 activity assay Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.9.3 7
-
 2'(3')-O-(2,4,6-trinitrophenyl)-ATP binding to wild-type and mutant SPS Escherichia coli
2.7.9.3 8
-
 activity assay Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.9.3 ATP
-
 Escherichia coli

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.9.3 Escherichia coli wild-type enzyme
-
 5.2
2.7.9.3 Escherichia coli mutant SPS262
-
 5.78

General Information

EC Number General Information Comment Organism
2.7.9.3 physiological function selenophosphate synthetase is a key enzyme of the selenium pathway in the cell Escherichia coli